TBB2A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TBB2A_MOUSE
• UniProt AC: Q7TMM9
• Protein Name: Tubulin beta-2A chain
• Gene Name: Tubb2a
• Organism: Mus musculus (Mouse).
• Sequence Length: 445
• Subcellular Localization: Cytoplasm, cytoskeleton.
• Protein Description: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity)..
• Protein Sequence: MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYSIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	S-nitrosocysteine	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	-
12	S-palmitoylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	28526873
12	S-nitrosylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	22588120
12	Glutathionylation	VHIQAGQCGNQIGAK EEEECCCCCCCHHHH	5.60	24333276
25	Phosphorylation	AKFWEVISDEHGIDP HHHHEHHHCCCCCCC	41.96	26370283
33	Phosphorylation	DEHGIDPTGSYHGDS CCCCCCCCCCCCCCC	34.70	29899451
35	Phosphorylation	HGIDPTGSYHGDSDL CCCCCCCCCCCCCCC	19.21	19060867
36	Phosphorylation	GIDPTGSYHGDSDLQ CCCCCCCCCCCCCCE	15.92	22817900
36	Nitration	GIDPTGSYHGDSDLQ CCCCCCCCCCCCCCE	15.92	-
40	Phosphorylation	TGSYHGDSDLQLERI CCCCCCCCCCEEEEE	44.83	21183079
46	Methylation	DSDLQLERINVYYNE CCCCEEEEEEEEEEH	34.08	26542105
51	Nitration	LERINVYYNEAAGNK EEEEEEEEEHHCCCC	11.40	-
58	Acetylation	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	22826441
58	Ubiquitination	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	27667366
58	Succinylation	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	22790023
58	Succinylation	YNEAAGNKYVPRAIL EEHHCCCCCCCEEEE	46.86	-
72	Phosphorylation	LVDLEPGTMDSVRSG EEECCCCCCCCCCCC	28.64	20415495
75	Phosphorylation	LEPGTMDSVRSGPFG CCCCCCCCCCCCCCC	14.49	22817900
78	Phosphorylation	GTMDSVRSGPFGQIF CCCCCCCCCCCCCCC	48.97	22817900
95	Phosphorylation	DNFVFGQSGAGNNWA CCEEECCCCCCCCCC	30.87	26745281
106	Phosphorylation	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	12692561
106	Nitration	NNWAKGHYTEGAELV CCCCCCCCCCHHHHH	18.37	-
107	Phosphorylation	NWAKGHYTEGAELVD CCCCCCCCCHHHHHH	23.44	12692561
115	Phosphorylation	EGAELVDSVLDVVRK CHHHHHHHHHHHHHH	19.66	27600695
124	Phosphorylation	LDVVRKESESCDCLQ HHHHHHHCCCCCCCC	37.53	20139300
126	Phosphorylation	VVRKESESCDCLQGF HHHHHCCCCCCCCCE	25.24	22817900
166	Phosphorylation	YPDRIMNTFSVMPSP CCCCCCHHEECCCCC	10.41	-
168	Phosphorylation	DRIMNTFSVMPSPKV CCCCHHEECCCCCCC	18.57	-
172	Phosphorylation	NTFSVMPSPKVSDTV HHEECCCCCCCCCCE	21.18	19737024
208	Phosphorylation	SIDNEALYDICFRTL EECHHHHHHHHHHEE	15.43	-
216	Ubiquitination	DICFRTLKLTTPTYG HHHHHEECCCCCCCC	43.08	-
218	Phosphorylation	CFRTLKLTTPTYGDL HHHEECCCCCCCCCH	29.19	19060867
219	Phosphorylation	FRTLKLTTPTYGDLN HHEECCCCCCCCCHH	24.86	22817900
221	Phosphorylation	TLKLTTPTYGDLNHL EECCCCCCCCCHHHH	37.74	19060867
222	Phosphorylation	LKLTTPTYGDLNHLV ECCCCCCCCCHHHHH	15.17	-
222	Nitration	LKLTTPTYGDLNHLV ECCCCCCCCCHHHHH	15.17	-
234	Phosphorylation	HLVSATMSGVTTCLR HHHHHHHCCCHHHHH	26.25	22006019
239	S-palmitoylation	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	28526873
239	Glutathionylation	TMSGVTTCLRFPGQL HHCCCHHHHHCCCCC	1.55	24333276
252	Acetylation	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	15614837
252	Ubiquitination	QLNADLRKLAVNMVP CCCHHHHHHHHHCCC	48.36	27667366
274	Phosphorylation	MPGFAPLTSRGSQQY CCCCCCCCCCCCHHH	18.47	21082442
275	Phosphorylation	PGFAPLTSRGSQQYR CCCCCCCCCCCHHHH	42.18	25177544
278	Phosphorylation	APLTSRGSQQYRALT CCCCCCCCHHHHEEE	17.01	26239621
281	Phosphorylation	TSRGSQQYRALTVPE CCCCCHHHHEEEHHH	7.10	23984901
285	Phosphorylation	SQQYRALTVPELTQQ CHHHHEEEHHHHHHH	32.79	-
290	Phosphorylation	ALTVPELTQQMFDSK EEEHHHHHHHHHCCC	18.32	-
296	Phosphorylation	LTQQMFDSKNMMAAC HHHHHHCCCCCHHHC	18.05	20139300
297	Ubiquitination	TQQMFDSKNMMAACD HHHHHCCCCCHHHCC	51.19	22790023
303	S-nitrosylation	SKNMMAACDPRHGRY CCCCHHHCCCCCCCC	5.55	19101475
303	S-palmitoylation	SKNMMAACDPRHGRY CCCCHHHCCCCCCCC	5.55	28526873
303	S-nitrosocysteine	SKNMMAACDPRHGRY CCCCHHHCCCCCCCC	5.55	-
303	Glutathionylation	SKNMMAACDPRHGRY CCCCHHHCCCCCCCC	5.55	24333276
312	Phosphorylation	PRHGRYLTVAAIFRG CCCCCCHHHHHHHCC	10.12	22817900
318	Methylation	LTVAAIFRGRMSMKE HHHHHHHCCCCCHHH	26.20	-
322	Phosphorylation	AIFRGRMSMKEVDEQ HHHCCCCCHHHHHHH	25.91	26370283
324	Ubiquitination	FRGRMSMKEVDEQML HCCCCCHHHHHHHHH	47.48	27667366
336	Ubiquitination	QMLNVQNKNSSYFVE HHHHCCCCCCCHHEE	40.91	-
338	Phosphorylation	LNVQNKNSSYFVEWI HHCCCCCCCHHEEEC	28.20	26745281
339	Phosphorylation	NVQNKNSSYFVEWIP HCCCCCCCHHEEECC	31.80	25521595
340	Phosphorylation	VQNKNSSYFVEWIPN CCCCCCCHHEEECCC	16.09	25521595
350	Ubiquitination	EWIPNNVKTAVCDIP EECCCCCCEEECCCC	32.65	-
354	S-nitrosylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	22588120
354	S-palmitoylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	28526873
354	Glutathionylation	NNVKTAVCDIPPRGL CCCCEEECCCCCCCC	3.49	24333276
362	Ubiquitination	DIPPRGLKMSATFIG CCCCCCCCEEEEECC	33.36	-
379	Ubiquitination	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	-
379	Acetylation	TAIQELFKRISEQFT HHHHHHHHHHHHHHH	62.54	7354907
382	Phosphorylation	QELFKRISEQFTAMF HHHHHHHHHHHHHHH	29.40	22817900
386	Phosphorylation	KRISEQFTAMFRRKA HHHHHHHHHHHHHHH	19.53	23684622
438	5-glutamyl polyglutamate	DEQGEFEEEEGEDEA HCCCCCCHHCCCCCC	67.67	-
438	Formation of an isopeptide bond	DEQGEFEEEEGEDEA HCCCCCCHHCCCCCC	67.67	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
172	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
172	S	Phosphorylation	Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TBB2A_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of TBB2A_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.